GREEN FLUORESCENT PROTEIN, APOPTOSIS REGULATOR BAX
Keywords
APOPTOSIS / PROGRAMMED CELL DEATH / BCL-2 FAMILY / CHIMERA
Function / homology
Function and homology information
T cell homeostatic proliferation / release of matrix enzymes from mitochondria / positive regulation of developmental pigmentation / protein insertion into mitochondrial membrane / BAX complex / B cell receptor apoptotic signaling pathway / positive regulation of reproductive process / positive regulation of motor neuron apoptotic process / regulation of mammary gland epithelial cell proliferation / spermatid differentiation ...T cell homeostatic proliferation / release of matrix enzymes from mitochondria / positive regulation of developmental pigmentation / protein insertion into mitochondrial membrane / BAX complex / B cell receptor apoptotic signaling pathway / positive regulation of reproductive process / positive regulation of motor neuron apoptotic process / regulation of mammary gland epithelial cell proliferation / spermatid differentiation / Activation, translocation and oligomerization of BAX / positive regulation of B cell apoptotic process / development of secondary sexual characteristics / NTRK3 as a dependence receptor / Sertoli cell proliferation / positive regulation of apoptotic DNA fragmentation / B cell homeostatic proliferation / glycosphingolipid metabolic process / positive regulation of mitochondrial membrane permeability involved in apoptotic process / retinal cell programmed cell death / B cell negative selection / BAK complex / apoptotic process involved in blood vessel morphogenesis / mitochondrial fragmentation involved in apoptotic process / negative regulation of endoplasmic reticulum calcium ion concentration / regulation of mitochondrial membrane permeability involved in programmed necrotic cell death / apoptotic process involved in embryonic digit morphogenesis / Release of apoptotic factors from the mitochondria / mitochondrial permeability transition pore complex / post-embryonic camera-type eye morphogenesis / establishment or maintenance of transmembrane electrochemical gradient / apoptotic process involved in mammary gland involution / Transcriptional regulation by RUNX2 / positive regulation of apoptotic process involved in mammary gland involution / regulation of nitrogen utilization / B cell apoptotic process / positive regulation of endoplasmic reticulum unfolded protein response / endoplasmic reticulum calcium ion homeostasis / fertilization / positive regulation of epithelial cell apoptotic process / calcium ion transport into cytosol / motor neuron apoptotic process / channel activity / mitochondrial fusion / Bcl-2 family protein complex / epithelial cell apoptotic process / myeloid cell homeostasis / BH domain binding / execution phase of apoptosis / hypothalamus development / positive regulation of calcium ion transport into cytosol / thymocyte apoptotic process / pore complex / odontogenesis of dentin-containing tooth / negative regulation of peptidyl-serine phosphorylation / BH3 domain binding / germ cell development / positive regulation of IRE1-mediated unfolded protein response / positive regulation of release of cytochrome c from mitochondria / apoptotic mitochondrial changes / TP53 Regulates Transcription of Genes Involved in Cytochrome C Release / vagina development / B cell homeostasis / negative regulation of mitochondrial membrane potential / negative regulation of apoptotic signaling pathway / intrinsic apoptotic signaling pathway by p53 class mediator / extrinsic apoptotic signaling pathway via death domain receptors / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / response to axon injury / blood vessel remodeling / ectopic germ cell programmed cell death / cellular response to unfolded protein / Pyroptosis / supramolecular fiber organization / negative regulation of fibroblast proliferation / extrinsic apoptotic signaling pathway / positive regulation of intrinsic apoptotic signaling pathway / ovarian follicle development / release of sequestered calcium ion into cytosol / extrinsic apoptotic signaling pathway in absence of ligand / homeostasis of number of cells within a tissue / response to salt stress / Hsp70 protein binding / intrinsic apoptotic signaling pathway / bioluminescence / positive regulation of release of sequestered calcium ion into cytosol / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / release of cytochrome c from mitochondria / regulation of mitochondrial membrane potential / negative regulation of protein binding / generation of precursor metabolites and energy / kidney development / response to gamma radiation / apoptotic signaling pathway / neuron migration / positive regulation of protein-containing complex assembly / response to toxic substance / cellular response to virus / cerebral cortex development / intrinsic apoptotic signaling pathway in response to DNA damage Similarity search - Function
Blc2-like / Apoptosis Regulator Bcl-x / Apoptosis regulator, Bcl-2, BH3 motif, conserved site / Apoptosis regulator, Bcl-2 family BH3 motif signature. / Apoptosis regulator, Bcl-2, BH1 motif, conserved site / Apoptosis regulator, Bcl-2 family BH1 motif signature. / Apoptosis regulator, Bcl-2, BH2 motif, conserved site / Apoptosis regulator, Bcl-2 family BH2 motif signature. / BCL (B-Cell lymphoma); contains BH1, BH2 regions / Bcl-2 family ...Blc2-like / Apoptosis Regulator Bcl-x / Apoptosis regulator, Bcl-2, BH3 motif, conserved site / Apoptosis regulator, Bcl-2 family BH3 motif signature. / Apoptosis regulator, Bcl-2, BH1 motif, conserved site / Apoptosis regulator, Bcl-2 family BH1 motif signature. / Apoptosis regulator, Bcl-2, BH2 motif, conserved site / Apoptosis regulator, Bcl-2 family BH2 motif signature. / BCL (B-Cell lymphoma); contains BH1, BH2 regions / Bcl-2 family / Bcl-2, Bcl-2 homology region 1-3 / Bcl2-like / Apoptosis regulator proteins, Bcl-2 family / BCL2-like apoptosis inhibitors family profile. / Bcl-2-like superfamily / Green Fluorescent Protein / Green fluorescent protein / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / Beta Barrel / Orthogonal Bundle / Mainly Beta / Mainly Alpha Similarity search - Domain/homology
SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
Mass: 18.015 Da / Num. of mol.: 84 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE SEQUENCE OF GFP IS AS DESCRIBED IN SUZUKI ET AL. (2010) ACTA CRYS D 66, 1059, BEARING THE EXTRA ...THE SEQUENCE OF GFP IS AS DESCRIBED IN SUZUKI ET AL. (2010) ACTA CRYS D 66, 1059, BEARING THE EXTRA MUTATION, A206N BAX TRUNCATED TO LEAVE ALPHA2 TO ALPHA5, MUTATIONS S62C, S126C. GFP AND BAX CRYSTALLIZED AS A SINGLE FUSION PROTEIN. 1000 HAS BEEN ADDED TO THE SEQUENCE NUMBERING OF BAX TO PRESERVE UNP NUMBERING.
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 3.75 Å3/Da / Density % sol: 67.22 % / Description: NONE
Crystal grow
Details: 10% PEG3350, 20% MPD, 0.5% CHAPS, 0.1 M TRIS PH 8.0
Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.9537 Å / Relative weight: 1
Reflection
Resolution: 3→19.9 Å / Num. obs: 41413 / % possible obs: 99.5 % / Observed criterion σ(I): -3 / Redundancy: 20.7 % / Biso Wilson estimate: 82.07 Å2 / Rmerge(I) obs: 0.1731 / Net I/σ(I): 17.74
Reflection shell
Resolution: 3→3.1 Å / Redundancy: 17.5 % / Rmerge(I) obs: 1.731 / Mean I/σ(I) obs: 2.26 / % possible all: 95.7
-
Processing
Software
Name
Version
Classification
PHENIX
(PHENIX.REFINE)
refinement
XDS
datareduction
XDS
datascaling
PHASER
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.998→19.959 Å / SU ML: 0.32 / σ(F): 1.99 / Phase error: 31.34 / Stereochemistry target values: ML Details: CONSTRUCT USED FOR CRYSTALLISATION CONSISTED OF GFP FUSED TO BAX AS DESCRIBED IN SUZUKI ET AL. (2010) ACTA CRYS D 66, 1059.
Rfactor
Num. reflection
% reflection
Rfree
0.246
2071
5 %
Rwork
0.2149
-
-
obs
0.2165
41413
99.38 %
Solvent computation
Shrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 51.524 Å2 / ksol: 0.263 e/Å3
Displacement parameters
Biso mean: 120.51 Å2
Baniso -1
Baniso -2
Baniso -3
1-
2.8299 Å2
0 Å2
0 Å2
2-
-
2.8299 Å2
0 Å2
3-
-
-
-5.6597 Å2
Refinement step
Cycle: LAST / Resolution: 2.998→19.959 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
9464
0
0
84
9548
Refine LS restraints
Refine-ID
Type
Dev ideal
Number
X-RAY DIFFRACTION
f_bond_d
0.009
9676
X-RAY DIFFRACTION
f_angle_d
1.39
13072
X-RAY DIFFRACTION
f_dihedral_angle_d
15.087
3544
X-RAY DIFFRACTION
f_chiral_restr
0.112
1404
X-RAY DIFFRACTION
f_plane_restr
0.004
1696
Refine LS restraints NCS
Ens-ID
Dom-ID
Auth asym-ID
Number
Refine-ID
Type
Rms dev position (Å)
1
1
A
1799
X-RAY DIFFRACTION
POSITIONAL
1
2
B
1799
X-RAY DIFFRACTION
POSITIONAL
0.223
1
3
C
1799
X-RAY DIFFRACTION
POSITIONAL
0.225
1
4
D
1799
X-RAY DIFFRACTION
POSITIONAL
0.111
2
1
A
548
X-RAY DIFFRACTION
POSITIONAL
2
2
B
548
X-RAY DIFFRACTION
POSITIONAL
0.021
2
3
C
548
X-RAY DIFFRACTION
POSITIONAL
0.022
2
4
D
548
X-RAY DIFFRACTION
POSITIONAL
0.007
LS refinement shell
Resolution (Å)
Rfactor Rfree
Num. reflection Rfree
Rfactor Rwork
Num. reflection Rwork
Refine-ID
% reflection obs (%)
2.9984-3.0679
0.3656
107
0.3547
2478
X-RAY DIFFRACTION
94
3.0679-3.1444
0.3242
210
0.3099
2568
X-RAY DIFFRACTION
100
3.1444-3.229
0.3685
109
0.2763
2657
X-RAY DIFFRACTION
100
3.229-3.3236
0.3306
108
0.2731
2646
X-RAY DIFFRACTION
100
3.3236-3.4304
0.3225
103
0.2473
2675
X-RAY DIFFRACTION
100
3.4304-3.5523
0.2854
209
0.2445
2569
X-RAY DIFFRACTION
100
3.5523-3.6937
0.3642
106
0.2334
2668
X-RAY DIFFRACTION
100
3.6937-3.8607
0.2652
102
0.2314
2688
X-RAY DIFFRACTION
100
3.8607-4.0626
0.269
211
0.2097
2552
X-RAY DIFFRACTION
100
4.0626-4.3147
0.2098
105
0.1919
2667
X-RAY DIFFRACTION
100
4.3147-4.644
0.1842
101
0.1696
2675
X-RAY DIFFRACTION
100
4.644-5.1043
0.1956
205
0.1654
2587
X-RAY DIFFRACTION
100
5.1043-5.8267
0.2796
101
0.1996
2661
X-RAY DIFFRACTION
100
5.8267-7.2813
0.231
102
0.2266
2681
X-RAY DIFFRACTION
100
7.2813-19.9592
0.2039
192
0.1998
2570
X-RAY DIFFRACTION
98
Refinement TLS params.
Method: refined / Refine-ID: X-RAY DIFFRACTION
ID
L11 (°2)
L12 (°2)
L13 (°2)
L22 (°2)
L23 (°2)
L33 (°2)
S11 (Å °)
S12 (Å °)
S13 (Å °)
S21 (Å °)
S22 (Å °)
S23 (Å °)
S31 (Å °)
S32 (Å °)
S33 (Å °)
T11 (Å2)
T12 (Å2)
T13 (Å2)
T22 (Å2)
T23 (Å2)
T33 (Å2)
Origin x (Å)
Origin y (Å)
Origin z (Å)
1
0.0498
-0.0009
0.019
0.0309
0.0099
0.0261
-0.0241
0.1045
-0.0535
-0.0223
-0.0383
-0.0212
-0.0238
0.0694
-0.0356
1.2765
-0.4146
0.1666
0.2384
-0.0782
0.3127
14.5202
102.1189
103.9046
2
0.0389
-0.0185
0.0045
0.0236
-0.0048
0.0382
-0.047
-0.1196
0.0881
0.0122
-0.0234
-0.0044
0.085
0.2035
-0.0696
0.6942
0.6282
-0.0913
0.7536
-0.0031
0.3502
14.5013
92.4246
30.2147
3
0.0187
0.0067
0.0183
0.0524
0.0079
0.0409
-0.0315
0.0364
-0.0381
-0.11
0.05
0.0388
-0.2535
0.0339
0.0014
0.9775
0.3701
0.0371
0.0606
0.0406
0.6445
31.1308
63.6067
135.2657
4
0.0624
0.0185
-0.0226
0.0461
-0.016
0.0149
0.0454
0.0213
0.0122
0.0967
-0.0544
0.0103
-0.1039
0.0877
-0.0227
-0.1656
0.4455
-0.0369
1.1744
-0.1724
0.6591
39.5524
58.7886
61.5724
5
-0.0018
-0.001
0.0015
0.0043
0.0042
0.0034
0.0585
0.0818
0.0567
0.0057
0.1131
0.099
0.0154
0.1163
-0
1.1897
0.192
-0.0236
1.0481
0.0933
0.7476
14.3873
97.0167
67.0126
6
0.0077
-0.0043
-0.0095
0.0019
0.002
0.0067
0.1256
-0.0392
-0.1049
0.0432
0.0423
0.0062
-0.1035
0.047
0
1.0241
0.2132
-0.0403
0.9144
0.0942
0.6982
35.0428
61.2253
98.5901
Refinement TLS group
ID
Refine-ID
Refine TLS-ID
Selection details
1
X-RAY DIFFRACTION
1
CHAINAANDRESID1:230
2
X-RAY DIFFRACTION
2
CHAINBANDRESID1:230
3
X-RAY DIFFRACTION
3
CHAINCANDRESID1:230
4
X-RAY DIFFRACTION
4
CHAINDANDRESID1:230
5
X-RAY DIFFRACTION
5
CHAINAORCHAINBANDRESID1053:1125
6
X-RAY DIFFRACTION
6
CHAINCORCHAINDANDRESID1053:1125
+
About Yorodumi
-
News
-
Feb 9, 2022. New format data for meta-information of EMDB entries
New format data for meta-information of EMDB entries
Version 3 of the EMDB header file is now the official format.
The previous official version 1.9 will be removed from the archive.
In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)
EMDB accession codes are about to change! (news from PDBe EMDB page)
The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
The EM Navigator/Yorodumi systems omit the EMD- prefix.
Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator
Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.
Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi